Evidence map›Paper›PMID 21540185›Full record

ArticleThe Journal of biological chemistry2011

The acylation state of surface lipoproteins of mollicute Acholeplasma laidlawii.

Marina V Serebryakova, Irina A Demina, Maria A Galyamina, Ilya G Kondratov, Valentina G Ladygina, Vadim M Govorun

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.5field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
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  7. Identification of the Lyso-FormJournal of bacteriology · 2017
    Article
  8. Article
  9. Article
  10. Article
  11. N-acylation of lipoproteins: not when sour.Journal of bacteriology · 2012
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. The iron-regulated staphylococcal lipoproteins.Frontiers in cellular and infection microbiology · 2012
    Review
  17. Article
  18. Article
  19. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Marina V SerebryakovaInstitute of Physico-Chemical Medicine, Federal Medico-Biological Agency, Moscow 119992, Russia. mserebr@mail.ru
Irina A Demina
Maria A Galyamina
Ilya G Kondratov
Valentina G Ladygina
Vadim M Govorun
Federal Medical-Biological Agency · RUInstitute of Gene Biology · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Acylation of the N-terminal Cys residue is an essential, ubiquitous, and uniquely bacterial posttranslational modification that allows anchoring of proteins to the lipid membrane. In gram-negative bacteria, acylation proceeds through three sequential steps requiring lipoprotein diacylglyceryltransferase, lipoprotein signal peptidase, and finally lipoprotein N-acyltransferase. The apparent lack of genes coding for recognizable homologs of lipoprotein N-acyltransferase in gram-positive bacteria and Mollicutes suggests that the final step of the protein acylation process may be absent in these organisms. In this work, we monitored the acylation state of eight major lipoproteins of the mollicute Acholeplasma laidlawii using a combination of standard two-dimensional gel electrophoresis protein separation, blotting to nitrocellulose membranes, and MALDI-MS identification of modified N-terminal tryptic peptides. We show that for each A. laidlawii lipoprotein studied a third fatty acid in an amide linkage on the N-terminal Cys residue is present, whereas diacylated species were not detected. The result thus proves that A. laidlawii encodes a lipoprotein N-acyltransferase activity. We hypothesize that N-acyltransferases encoded by genes non-homologous to N-acyltransferases of gram-negative bacteria are also present in other mollicutes and gram-positive bacteria.

Indexed as

AcetylationAcholeplasma laidlawiiAcyltransferasesBacterial ProteinsLipoproteinsProtein Processing, Post-TranslationalAcyltransferasesBacterial ProteinsLipoproteins

Identifiers

PMID21540185
PMCPMC3123044
OpenAlexW2013792342

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.